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Expert Rev Mol Diagn. 2017 Oct;17(10):897-904. doi: 10.1080/14737159.2017.1368389. Epub 2017 Sep 8.

Applications of the real-time quaking-induced conversion assay in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies.

Author information

1
a Department of Neurology , University Medical Center Göttingen and the German Center for Neurodegenerative Diseases (DZNE) , Göttingen , Germany.
2
b Department of Neuropathology , Center for Networked Biomedical Research on Neurodegenerative Diseases (CIBERNED) , Barcelona , Spain.

Abstract

The development of in vitro protein misfolding amplification assays for the detection and analysis of abnormally folded proteins, such as proteinase K resistant prion protein (PrPres) was a major innovation in the prion field. In prion diseases, these types of assays imitate the pathological conversion of the cellular PrP (PrPC) into a proteinase resistant associated conformer or amyloid, called PrPres. Areas covered: The most prominent protein misfolding amplification assays are the protein misfolding cyclic amplification (PMCA), which is based on sonication and the real-time quaking-induced conversion (RT-QuIC) technique based on shaking. The more recently established RT-QuIC is fully automatic and enables the monitoring of misfolded protein aggregates in real-time by using a fluorescent dye. Expert commentary: RT-QuIC is a very robust and highly reproducible test system which is applicable in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies.

KEYWORDS:

Real-time quaking-induced conversion; aggregation; prion protein; protein misfolding; sporadic Creutzfeldt-Jakob disease

PMID:
28817974
DOI:
10.1080/14737159.2017.1368389
[Indexed for MEDLINE]

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